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Database: UniProt
Entry: A0A0N5CN35_THECL
LinkDB: A0A0N5CN35_THECL
Original site: A0A0N5CN35_THECL 
ID   A0A0N5CN35_THECL        Unreviewed;       237 AA.
AC   A0A0N5CN35;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE            EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN   ORFNames=TCLT_LOCUS1580 {ECO:0000313|EMBL:VDM97095.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000157901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000157901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM97095.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UYYF01000216; VDM97095.1; -; Genomic_DNA.
DR   STRING; 103827.A0A0N5CN35; -.
DR   WBParaSite; TCLT_0000157901-mRNA-1; TCLT_0000157901-mRNA-1; TCLT_0000157901.
DR   OMA; TDMCKAL; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR   GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR   CDD; cd07995; TPK; 1.
DR   Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR   Gene3D; 2.60.120.320; Thiamin pyrophosphokinase, thiamin-binding domain; 1.
DR   InterPro; IPR006282; Thi_PPkinase.
DR   InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd.
DR   InterPro; IPR036371; TPK_B1-bd_sf.
DR   InterPro; IPR007371; TPK_catalytic.
DR   InterPro; IPR036759; TPK_catalytic_sf.
DR   NCBIfam; TIGR01378; thi_PPkinase; 1.
DR   PANTHER; PTHR13622; THIAMIN PYROPHOSPHOKINASE; 1.
DR   PANTHER; PTHR13622:SF8; THIAMIN PYROPHOSPHOKINASE 1; 1.
DR   Pfam; PF04265; TPK_B1_binding; 1.
DR   Pfam; PF04263; TPK_catalytic; 1.
DR   SMART; SM00983; TPK_B1_binding; 1.
DR   SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
DR   SUPFAM; SSF63862; Thiamin pyrophosphokinase, substrate-binding domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          148..226
FT                   /note="Thiamin pyrophosphokinase thiamin-binding"
FT                   /evidence="ECO:0000259|SMART:SM00983"
SQ   SEQUENCE   237 AA;  26137 MW;  63FAA9431C020C05 CRC64;
     MSSQLFSENF GVLWVNSPPE NLSQKLTKRL WNEGVFRACT DGAANFIMPL VQNEHYLTPN
     LISGDFDSIT TKARNFFDSQ AEFVETSDPD YTDMTKSLKI IAGRINNKKL DMSKLIILGG
     LCGRFDHVLS SLHSLLQFSA CDAMIIDGYN LLTILPKGST HLNLTGRNAF STGMCGVIPF
     VQEKTMASTV GLKWNLHNTE LAFGKLISSS NEVVCDRITI TTTAPVVFTA ELKQGVM
//
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